HIP_RHOGL
ID HIP_RHOGL Reviewed; 57 AA.
AC P38589;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=High-potential iron-sulfur protein;
DE Short=HiPIP;
GN Name=hip;
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=8215406; DOI=10.1006/abbi.1993.1503;
RA Ambler R.P., Meyer T.E., Kamen M.D.;
RT "Amino acid sequence of a high redox potential ferredoxin (HiPIP) from the
RT purple phototrophic bacterium Rhodopila globiformis, which has the highest
RT known redox potential of its class.";
RL Arch. Biochem. Biophys. 306:215-222(1993).
CC -!- FUNCTION: Specific class of high-redox-potential 4Fe-4S ferredoxins.
CC Functions in anaerobic electron transport in most purple and in some
CC other photosynthetic bacteria and in at least one genus (Paracoccus) of
CC halophilic, denitrifying bacteria.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is +450 mV.;
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP)
CC family. {ECO:0000255|PROSITE-ProRule:PRU00705}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S38752; S38752.
DR AlphaFoldDB; P38589; -.
DR SMR; P38589; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR Gene3D; 4.10.490.10; -; 1.
DR InterPro; IPR000170; High_potential_FeS_prot.
DR InterPro; IPR036369; HIPIP_sf.
DR Pfam; PF01355; HIPIP; 1.
DR SUPFAM; SSF57652; SSF57652; 1.
DR PROSITE; PS51373; HIPIP; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Transport.
FT CHAIN 1..57
FT /note="High-potential iron-sulfur protein"
FT /id="PRO_0000220426"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT BINDING 33
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
SQ SEQUENCE 57 AA; 6223 MW; 4DEFB25397DB8ABF CRC64;
QDKIDPKMVQ YQDSPKDGNK CSTCVNFEAP SSCKIVAGKI SPNGWCIAYA PMEDKKG